Jacalin interacts with Asn-linked glycopeptides containing multi-antennary oligosaccharide structure with terminal alpha-linked galactose.
The carbohydrate binding properties of jacalin lectin were examined using RAF9 cell-derived D-[6-3H]glucosamine-radiolabeled total glycopeptides containing N-linked and O-linked oligosaccharides. The binding of N-linked glycopeptides to jacalin was abolished by treatment of alpha-galactosidase whereas O-linked glycopeptides were still bound lectin after this treatment. The removal of O-linked oligosaccharides by mild alkaline/borohydride treatment completely eliminated the lectin binding of alpha-galactosidase treated glycopeptides. These results demonstrate that jacalin interacts with cellular glycopeptides containing N-linked oligosaccharides with terminal alpha-galactose residues as well as glycopeptides containing O-linked oligosaccharides.
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Korea Research Institute of Bioscience and Biotechnology, Animal Cell and Medical Glycobiology Laboratory, Yusung, Taejon, South Korea. sido@kribb4680.kribb.re.kr
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D000818:Animals; D001216:Asparagine / Q000378:metabolism*; D005690:Galactose / Q000378:metabolism*; D006023:Glycoproteins / Q000378:metabolism*; D037102:Lectins / Q000378:metabolism*; D051379:Mice; D009844:Oligosaccharides / Q000378:metabolism*; D037121:Plant Lectins; D014407:Tumor Cells, Cultured
D006023:Glycoproteins; D037102:Lectins; D009844:Oligosaccharides; D037121:Plant Lectins; C043696:jacalin; D001216:Asparagine; D005690:Galactose